| 1.Research Institution | @ | The University of Tokyo |
| @ | ||
| 2.Research Area | @ | Life Sciences |
| @ | ||
| 3.Research Field | @ | Structure and Functional Control Mechanism of Biomolecules (Structural Biology and Functional Molecules) |
| @ | ||
| 4.Term of Project | @ | FY1996`FY2000 |
| @ | ||
| 5.Project Number | @ | 96L00505 |
| @ | ||
| 6.Title of Project | @ | Structural Change of Signal-transducing Proteins Induced by Ligand Binding: Its Significance in Signal Generation |
| Name | Institution,Department | Title of Position |
| Toshiaki, KATADA | The University of Tokyo, Grad. Sch. of Pharmaceut. Sci., | Professor |
8.Core Members
| Names | Institution,Department | Title of Position |
| Yoshinori, SATOW | The University of Tokyo, Grad. Sch. of Pharmaceut. Sci., | Professor |
| Ichio, SHIMADA | The University of Tokyo, Grad. Sch. of Pharmaceut. Sci., | Professor |
| Hiroyuki, ARAI | The University of Tokyo, Grad. Sch. of Pharmaceut. Sci., | Professor |
9.Cooperating Researchers
| Names | Institution,Department | Title of Position |
| Hiroshi, NISHINA | The University of Tokyo, Grad. Sch. of Pharmaceut. Sci., | Associate Professor |
| Shin-ichi, HOSHINO | The University of Tokyo, Grad. Sch. of Pharmaceut. Sci., | Research fellow |
| Kenji, KONTANI | The University of Tokyo, Grad. Sch. of Pharmaceut. Sci., | Research fellow |
10.Summary of Research Results
|
In the present study, we analyzed the structures and functions of various proteins involved in signal-transduction systems. Three-dimensional structural analysis by X-ray crystallography and NMR was performed especially for the signal-transduction processes of ligand-protein and protein-protein interaction. We obtained the following new findings. 1. A novel G protein GSPT was identified as the eukaryotic polypeptide releasing factor eRF3. GSPT/eRF3 functioned not only in translation termination but also in mRNA degradation. The N domain of eRF3 associated with PABP to unmask the poly(A) tail of mRNAs for their degradation. Novel molecules were identified as binding proteins for the small GTPase Rab5, which was also capable of binding to the p110/p85 subtype of phosphoinositide 3-OH kinases. The Rab5-binding proteins were transferred into nucleus at G2-M phase in a manner dependent on GTP-bound Rab5. 2. Three-dimensional structural studies by X-ray crystallography were carried on the liganded proteins of glutathione S-transferase, antibody Fab and Fv fragments, human renal dipeptidase, Fabry disease enzyme of human -galactosidase. Large-scale expression systems were developed for the structural studies of human interleukin-6 receptor and 3-adregenic receptor. 3. By NMR analysis, we showed that stoichiometry of the Fc-sFcRII interactions 1:1. An extensive mapping of the sFcRII-binding site of Fc, which was performed by use of stable-isotope-assisted NMR spectroscopy, led us to conclude that sFcRII binds to the lower hinge and its spatial proximity of the IgG-Fc. We also developed a stable isotope-labeling method for glycans attached to glycoproteins and a method used for the identification of the interfaces of larger protein-protein complexes in solution. 4. Three-dimensional structural analysis by X-ray crystallography was performed on the subunit of PAF acetylhyrolase. The subunit was structurally quite similar to the trimeric G protein subunit. The LIS1/ subunit appeared to function in nuclear migration by interacting with multiple intracellular proteins. |
11.Key Words
(1)G proteinA(2)Translation terminationA(3)mRNA decay
(4)GlycoproteinA(5)AntibodyA(6)Recepror
(7)PAF acetylhydrolaseA(8)X-ray crystallographyA(9)NMR
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